• Preventive Nutrition and Food Science
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• 제1권1호
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• pp.53-58
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• 1996

The characterstics of the soy protein curd(eczyme-, HCI- and Ca-surd) were shown by scanning electron micrographs and gel electrophoreis. The emulsion stability of enzyme-curd showed high value in the range of pH 2~10and wide range of temperature(20~8$0^{\circ}C$). While at the isoelectric point(pH5.0), the emulsion stability of the HCI-and Ca-curd was decreased remarkably, and the emulsion stability of temperature was reduced quickly to the 60% and 40% at the 4$0^{\circ}C$. The foam stability of enzyme-curd was slightly higher than that HCI-and CA-curd in all ranges of pH and temperature. The feature of SEM of enzyme-cured produced degradation products faster than that of the HCI- and Ca-curd.

• Journal of Microbiology and Biotechnology
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• 제4권2호
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• pp.119-125
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• 1994

Steroid $\Delta^1$-dehydrogenase purified from hydrocortisone-induced cells of Arthrobacter simplex converted various 3-ketosteroids into their corresponding $\Delta^1$-dehydrogenated products. The transformation efficiencies depend upon the chemical structure of the steroids, especially length of the side chain at 17 position and hydroxyl groups at 11 and 17 positions. The Km values for androstenedione, the most favorable substrate examined, and hydrocortisone were 74 ${\mu}M$ and 294 ${\mu}M$, respectively. The optimum temperature and pH of the enzyme reaction were 35$^{\circ}C$ and pH 9, respectively, and the enzyme was relatively stable at the range from 20 to 35$^{\circ}C$ and from pH 5 to 10 after one hour of incubation. The enzyme activity was markedly inhibited in the presence of $Cu^{2+},\;Fe^{3+},\;Hg^{2+},\;Mo^{6+}$ ions, and somewhat inhibited by $Zn^{2+}$ and $Fe^{2+}$. $\alpha,\alpha'$-Dipyridyl that inhibits 9$\alpha$-hydroxylase and accumulates 1,4-androstadiene-3,17-dione from sterols revealed no inhibitory effect on this enzyme. EGTA showed inhibitory effect. $\beta$-Estradiol competitively inhibited the enzyme activity. Chemical modifications of the enzyme were attempted with several reagents. p-Hydroxymer-curibenzoate showed inhibition of the enzyme activity and protection of the substrate. This suggests that cysteine residue may be involved in the active site of the enzyme.

• Journal of Microbiology and Biotechnology
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• 제8권4호
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• pp.318-324
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• 1998

A ${\beta}$-galactosidase with high transgalactosylic activity was purified from a Bacillus species, registered as KFCC10855. The enzyme preparation showed a single protein band corresponding to a molecular mass of 150 kDa on SDS-PAGE and gave a single peak with the estimated molecular mass of 250 kDa on Sephacryl S-300 gel filtration, suggesting that the enzyme is a homodimeric protein. The amino acid and sugar analyses revealed that the enzyme is a glycoprotein, containing 19.2 weight percent of sugar moieties, and is much more abundant in hydrophilic amino acid residues than in hydrophobic residues, the mole ratio being about 2:1. The pI and optimum pH were determined to be 5.0 and 6.0, respectively. Having a temperature optimum at $70^{\circ}C$ for the hydrolysis of lactose, the enzyme showed good thermal stability. The activity of the enzyme preparation was markedly increased by the presence of exogenous Mg (II) and was decreased by the addition of EDTA. Among the metal ions examined, the most severely inhibitory effect was seen with Ag (I) and Hg (II). Further, results of protein modification by various chemical reagents implied that 1 cysteine, 1 histidine, and 2 methionine residues occur in certain critical sites of the enzyme, most likely including the active site. Enzyme kinetic parameters, measured for both hydrolysis and transgalactosylation of lactose, indicated that the enzyme has an excellent catalytic efficiency for formation of the transgalactosylic products in reaction mixtures containing high concentrations of the substrate.

• 식품산업과 영양
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• 제4권1호
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• pp.31-35
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• 1999

• Journal of Microbiology and Biotechnology
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• 제12권3호
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• pp.530-533
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• 2002

This paper describes the development of an enzymatic assay system for the identification of specific inhibitors of sortase, a transpeptidase that cleaves surface proteins of Cram-positive bacteria, from Staphylococcus aureus ATCC 6538p for antibacterial drug discovery. The coding region of the enzyme was amplified with the exception of the N-terminal membrane anchor sequence, cloned into a vector providing His-Patch-thioredoxin-tag at the N-terminus, expressed in Escherichia coli, and purified by metal chelate affinity chromatography. The enzyme activity was determined by quantifying increased fluorescence intensity upon cleavage of synthetic Dabcyl-QALPETGEE-Edans peptide. The results suggest that the developed in vitro assay system call be used in the search for sortase inhibitors In a short period of time.

• 펄프종이기술
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• 제45권6호
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• pp.78-87
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• 2013

Even though the notice No. 2010-11 of the Ministry of Food and Drug Safety Administration that has been applied to analyze the content of the water soluble residue eluted from multi-layer paperboard was abolished in 2011, its application for the analysis on evaporation residue is still valid. There are very high possibilities that the noticed existing method gives the misleading result on the evaporation residue due to the water soluble starch eluted from the multi-layer paperboard. The quantitative analysis on water-soluble residue with starch content correction has been carried in the study using UV/Vis spectroscopy and HPLC. The UV/Vis spectroscopy absorbance analysis showed the large amount of the oxidized starch obtained from the aqueous residue eluted out of the multi-layer paperboard after the iodine, ${\alpha}$-amylase reaction, and starch hydrolysis. The residual content decreased by the correction through the enzyme hydrolysis.

• Journal of the Korean Wood Science and Technology
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• 제47권3호
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• pp.371-380
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• 2019

Termites are pests that cause serious economic and cultural damage by digesting wood cellulose. Termites are arthropods and have an epidermis surrounded by a chitin layer. To maintain a healthy epidermis, termites have chitinase (${\beta}$-1,4-poly-N-acetyl glucosamidinase, EC 3.2.1.14), an enzyme that hydrolyzes the ${\beta}$-1,4 bond of chitin. In this study, the amino acid sequence of the gene, which is presumed to be termite chitinolytic enzyme (NCBI accession no. KC477099), was obtained from a transcriptomic analysis of Reticulitermes speratus KMT001 in Bukhan Mountain, Korea. An NCBI protein BLAST search confirmed that the protein is a glycoside hydrolase family 18 (GH18). The highest homology value found was 47%, with a chitinase from Araneus ventricosus. Phylogenetic analysis indicated that the KC477099 protein has the same origins as those of arthropods but has a very low similarity with other arthropod chitinases, resulting in separation at an early stage of evolution. The KC477099 protein contains two conserved motifs, which encode the general enzymatic characteristics of the GH18 group. The amino acid sequences $Asp^{156}-Trp^{157}-Glu^{158}$, which play an important role in the enzymatic activity of the GH18 group, were also present. This study suggests that the termite KC477099 protein is a new type of chitinase, which is evolutionarily distant from other insect chitinases.

• 한국식품과학회지
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• 제33권4호
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• pp.461-468
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• 2001

본 연구는 시판 건강보조식품 중 효소식품의 성분을 분석하고 그 제조공정을 조사하여 HACCP system에 근거한 품질관리 개선 방안을 수립하고자 하였다. 이를 위하여 시중에서 가장 많이 판매되고 있는 12종류의 효소식품을 대상으로 일반성분, 효소활성도 및 미생물과 아플라톡신의 오염 등을 측정하였다. 실험결과 효소식품의 제품포장에 표시된 일반성분함량과 실험치와 차이가 큰 것으로 나타났다. 효소식품의 가장 큰 유효성으로 알려진 효소활성의 측정결과에서도 ${\alpha}-amylase$의 경우, 최고 $1793\;{\mu}g/min$ g에서 최저 $159\;{\mu}g/min$ g으로 커다란 편차를 보였으며, ${\beta}-amylase$의 경우, 최고 $171\;{\mu}g/min$ g와 최저 $11\;{\mu}g/min$ g, 그리고 protease이 경우 최고 $27.57\;{\mu}g/min$ g와 최저 $0.18\;{\mu}g/min$ g으로 나타나 단지 ${\alpha}-amylase$와 protease의 활성이 양성일 경우 적합판정을 내리는 현 공전상의 규정에 문제가 있음을 알 수 있었다. 또한 규정상 대장균 군에 대하여 음성이여야 함에도 불구하고 효소식품의 반수가 대장균 군에 양성으로 나타났으며 일반세균수에 있어서도 $1.3{\times}10^5-1.2{\times}10^9$로 큰 차이를 보이고 있어 효소활성을 위해 저온살균공정을 거치는 이들 제품의 위생적 관리가 시급함을 알 수 있었다. 이에따라 위해요소 중점 관리기준(HACCP)을 작성하여 효소식품의 품질향상을 위한 관리지침을 수립하였다.

• Archives of Pharmacal Research
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• 제13권2호
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• pp.132-135
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• 1990

Polyhydroxystilbenes including resveratrol were reported to competitively inhibit monoamine oxidase-A-without structural relation with substrates and cynthetic inhibitors for the enzyme. We attempt to explore a plausible mechanism for their inhibitory activity on MAO-A. All the polyhydroxystilbenes tested showed the antioxidant activity on liver homogenate. Furthermore, the antioxidant activity turned out to closely correlate with the MAO-A inhibitory activity.

• 한국식품영양과학회지
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• 제22권3호
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• pp.273-279
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• 1993

박테리아 Bacillus sp. K-295G-7이 생산하는 두유응고효소 I 및 II에 의한 11S globulin (glycinin)의 가수분해 패턴을 조사하였다. 효소 I 과 II에 의한 acidic subunit의 응고시간은 약 4-5 분이었다. 전기 영동의 결과, acidic subunit (A$_3$, M.W=45,000)는 효소반응 2분 이내에 완전히 가수분해되어 분자량 16,000, 20,000의 새로운 band를 형성하였다. 한편 효소 II의 작용으로 약 30,000의 분자량을 가진 분해산물을 생성하였고 효소 I 과 II의 basic subunit 에 대한 가수분해 패턴은 유사하였다.